CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-003802
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Receptor-type tyrosine-protein phosphatase F 
Protein Synonyms/Alias
 Leukocyte common antigen related; LAR 
Gene Name
 PTPRF 
Gene Synonyms/Alias
 LAR 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
144IDMGPQLKVVEKARTubiquitination[1]
274MGAEELTKEDEMPVGubiquitination[1]
1295RTHSPSSKDEQSIGLubiquitination[1]
1303DEQSIGLKDSLLAHSubiquitination[1, 2, 3, 4]
1376NSNLEVNKPKNRYANubiquitination[1]
1572LERMKHEKTVDIYGHubiquitination[3]
1810WPEQGVPKTGEGFIDubiquitination[1]
Reference
 [1] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [2] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [3] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [4] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789] 
Functional Description
 Possible cell adhesion receptor. It possesses an intrinsic protein tyrosine phosphatase activity (PTPase). 
Sequence Annotation
 DOMAIN 33 123 Ig-like C2-type 1.
 DOMAIN 135 224 Ig-like C2-type 2.
 DOMAIN 232 314 Ig-like C2-type 3.
 DOMAIN 319 407 Fibronectin type-III 1.
 DOMAIN 413 506 Fibronectin type-III 2.
 DOMAIN 512 602 Fibronectin type-III 3.
 DOMAIN 606 703 Fibronectin type-III 4.
 DOMAIN 708 815 Fibronectin type-III 5.
 DOMAIN 817 910 Fibronectin type-III 6.
 DOMAIN 915 1008 Fibronectin type-III 7.
 DOMAIN 1011 1095 Fibronectin type-III 8.
 DOMAIN 1352 1607 Tyrosine-protein phosphatase 1.
 DOMAIN 1639 1898 Tyrosine-protein phosphatase 2.
 REGION 68 77 Heparin-binding (By similarity).
 REGION 1548 1554 Substrate binding (By similarity).
 ACT_SITE 1548 1548 Phosphocysteine intermediate (Probable).
 ACT_SITE 1839 1839 Phosphocysteine intermediate (By
 BINDING 1516 1516 Substrate (By similarity).
 BINDING 1592 1592 Substrate (By similarity).
 CARBOHYD 117 117 N-linked (GlcNAc...) (Potential).
 CARBOHYD 250 250 N-linked (GlcNAc...) (Potential).
 CARBOHYD 295 295 N-linked (GlcNAc...) (Potential).
 CARBOHYD 721 721 N-linked (GlcNAc...) (Potential).
 CARBOHYD 959 959 N-linked (GlcNAc...); atypical.
 CARBOHYD 966 966 N-linked (GlcNAc...).
 DISULFID 54 107 By similarity.
 DISULFID 156 207 By similarity.
 DISULFID 253 298 By similarity.  
Keyword
 3D-structure; Alternative splicing; Cell adhesion; Complete proteome; Disulfide bond; Glycoprotein; Heparin-binding; Hydrolase; Immunoglobulin domain; Membrane; Polymorphism; Protein phosphatase; Receptor; Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1907 AA 
Protein Sequence
MAPEPAPGRT MVPLVPALVM LGLVAGAHGD SKPVFIKVPE DQTGLSGGVA SFVCQATGEP 60
KPRITWMKKG KKVSSQRFEV IEFDDGAGSV LRIQPLRVQR DEAIYECTAT NSLGEINTSA 120
KLSVLEEEQL PPGFPSIDMG PQLKVVEKAR TATMLCAAGG NPDPEISWFK DFLPVDPATS 180
NGRIKQLRSG ALQIESSEES DQGKYECVAT NSAGTRYSAP ANLYVRVRRV APRFSIPPSS 240
QEVMPGGSVN LTCVAVGAPM PYVKWMMGAE ELTKEDEMPV GRNVLELSNV VRSANYTCVA 300
ISSLGMIEAT AQVTVKALPK PPIDLVVTET TATSVTLTWD SGNSEPVTYY GIQYRAAGTE 360
GPFQEVDGVA TTRYSIGGLS PFSEYAFRVL AVNSIGRGPP SEAVRARTGE QAPSSPPRRV 420
QARMLSASTM LVQWEPPEEP NGLVRGYRVY YTPDSRRPPN AWHKHNTDAG LLTTVGSLLP 480
GITYSLRVLA FTAVGDGPPS PTIQVKTQQG VPAQPADFQA EVESDTRIQL SWLLPPQERI 540
IMYELVYWAA EDEDQQHKVT FDPTSSYTLE DLKPDTLYRF QLAARSDMGV GVFTPTIEAR 600
TAQSTPSAPP QKVMCVSMGS TTVRVSWVPP PADSRNGVIT QYSVAYEAVD GEDRGRHVVD 660
GISREHSSWD LVGLEKWTEY RVWVRAHTDV GPGPESSPVL VRTDEDVPSG PPRKVEVEPL 720
NSTAVHVYWK LPVPSKQHGQ IRGYQVTYVR LENGEPRGLP IIQDVMLAEA QWRPEESEDY 780
ETTISGLTPE TTYSVTVAAY TTKGDGARSK PKIVTTTGAV PGRPTMMIST TAMNTALLQW 840
HPPKELPGEL LGYRLQYCRA DEARPNTIDF GKDDQHFTVT GLHKGTTYIF RLAAKNRAGL 900
GEEFEKEIRT PEDLPSGFPQ NLHVTGLTTS TTELAWDPPV LAERNGRIIS YTVVFRDINS 960
QQELQNITTD TRFTLTGLKP DTTYDIKVRA WTSKGSGPLS PSIQSRTMPV EQVFAKNFRV 1020
AAAMKTSVLL SWEVPDSYKS AVPFKILYNG QSVEVDGHSM RKLIADLQPN TEYSFVLMNR 1080
GSSAGGLQHL VSIRTAPDLL PHKPLPASAY IEDGRFDLSM PHVQDPSLVR WFYIVVVPID 1140
RVGGSMLTPR WSTPEELELD ELLEAIEQGG EEQRRRRRQA ERLKPYVAAQ LDVLPETFTL 1200
GDKKNYRGFY NRPLSPDLSY QCFVLASLKE PMDQKRYASS PYSDEIVVQV TPAQQQEEPE 1260
MLWVTGPVLA VILIILIVIA ILLFKRKRTH SPSSKDEQSI GLKDSLLAHS SDPVEMRRLN 1320
YQTPGMRDHP PIPITDLADN IERLKANDGL KFSQEYESID PGQQFTWENS NLEVNKPKNR 1380
YANVIAYDHS RVILTSIDGV PGSDYINANY IDGYRKQNAY IATQGPLPET MGDFWRMVWE 1440
QRTATVVMMT RLEEKSRVKC DQYWPARGTE TCGLIQVTLL DTVELATYTV RTFALHKSGS 1500
SEKRELRQFQ FMAWPDHGVP EYPTPILAFL RRVKACNPLD AGPMVVHCSA GVGRTGCFIV 1560
IDAMLERMKH EKTVDIYGHV TCMRSQRNYM VQTEDQYVFI HEALLEAATC GHTEVPARNL 1620
YAHIQKLGQV PPGESVTAME LEFKLLASSK AHTSRFISAN LPCNKFKNRL VNIMPYELTR 1680
VCLQPIRGVE GSDYINASFL DGYRQQKAYI ATQGPLAEST EDFWRMLWEH NSTIIVMLTK 1740
LREMGREKCH QYWPAERSAR YQYFVVDPMA EYNMPQYILR EFKVTDARDG QSRTIRQFQF 1800
TDWPEQGVPK TGEGFIDFIG QVHKTKEQFG QDGPITVHCS AGVGRTGVFI TLSIVLERMR 1860
YEGVVDMFQT VKTLRTQRPA MVQTEDQYQL CYRAALEYLG SFDHYAT 1907 
Gene Ontology
 GO:0005887; C:integral to plasma membrane; TAS:ProtInc.
 GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
 GO:0005001; F:transmembrane receptor protein tyrosine phosphatase activity; TAS:ProtInc.
 GO:0007155; P:cell adhesion; TAS:ProtInc.
 GO:0007185; P:transmembrane receptor protein tyrosine phosphatase signaling pathway; TAS:ProtInc. 
Interpro
 IPR003961; Fibronectin_type3.
 IPR007110; Ig-like_dom.
 IPR013783; Ig-like_fold.
 IPR013098; Ig_I-set.
 IPR003598; Ig_sub2.
 IPR000387; Tyr/Dual-sp_Pase.
 IPR016130; Tyr_Pase_AS.
 IPR000242; Tyr_Pase_rcpt/non-rcpt. 
Pfam
 PF00041; fn3
 PF07679; I-set
 PF00102; Y_phosphatase 
SMART
 SM00060; FN3
 SM00408; IGc2
 SM00194; PTPc 
PROSITE
 PS50853; FN3
 PS50835; IG_LIKE
 PS00383; TYR_PHOSPHATASE_1
 PS50056; TYR_PHOSPHATASE_2
 PS50055; TYR_PHOSPHATASE_PTP 
PRINTS
 PR00700; PRTYPHPHTASE.